Helix-Coil Stability Constants for the Naturally Occurring Amino Acids in Water. 11. Lysine Parameters from Random Poly(hydroxybutylglutamine-co-L-lysine) | Zendy

M. K. Dygert | Zendy; G. T. Taylor | Zendy; F. Cardinaux | Zendy; Harold A. Scheraga | Zendy

Open Access

Helix-Coil Stability Constants for the Naturally Occurring Amino Acids in Water. 11. Lysine Parameters from Random Poly(hydroxybutylglutamine-co-L-lysine)

Author(s) -

M. K. Dygert,

G. T. Taylor,

F. Cardinaux,

Harold A. Scheraga

Publication year - 1976

Publication title -

macromolecules

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.994

H-Index - 313

eISSN - 1520-5835

pISSN - 0024-9297

DOI - 10.1021/ma60053a021

Subject(s) - altmetrics , random coil , lysine , citation , icon , protein stability , computer science , social media , chemistry , information retrieval , nanotechnology , amino acid , library science , materials science , world wide web , biochemistry , protein secondary structure , programming language

The synthesis and characterization of water-soluble random copolymers containing L-lysine with N5-(4-hydroxybutyl)-L-glutamine, and the thermally induced helix-coil transitions of these copolymers in water, are described. The incorporation of L-lysine was found to decrease the helix content of the polymers at neutral pH. The Zimm-Bragg parameters sigma and s for the helix-coil transition in poly(L-lysine) in water were deduced from an analysis of the melting curves in the manner described in earlier papers. The computed values of s indicate that, in the temperature range of 0-60 degrees C, lysine has a tendency to destabilize helical sequences, this tendency being minimal at approximately 25 degrees C and increasing at lower and higher temperatures.

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